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 หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Relationship Between Invertase Enzyme Activities and Sucrose Accumulation in Sugarcane (Saccharum spp.)) ผู้เขียน: Bootsarin Tana,  ดร.สนธิชัย จันทร์เปรม, รองศาสตราจารย์ , Nongluck Tienseree, ดร.สุคันธรส ธาดากิตติสาร สื่อสิ่งพิมพ์:pdf AbstractThe sucrose content, and the activities of sugar metabolism enzymes—namely, soluble acid invertase (SAI), neutral invertase (NI) and cell wall invertase (CWI), of various developmental stages of the stem and the relationships among them were investigated in cultivated sugarcane (Saccharum officinarum L.), line 20-2248 and wild sugarcane S. spontaneum, line S98-244. Stems of both sugarcane species 6–12 mth after planting (MAP) stems were collected and examined with samples consisting of three parts of the internode—the top, middle and bottom—representing relatively immature, maturing and mature internodes, respectively. The results showed that sucrose was the main sugar in the two species. Sugarcane stems of the two species revealed different patterns of sucrose accumulation and activities of invertase (SAI, CWI and NI). The sucrose content of line 20-2248 increased from 6 to 12 MAP and was highest in the bottom part and decreased in the middle and top parts, respectively, whereas the sucrose content of line S98-244 decreased from 6 to 12 MAP and was highest in the middle part than in the lower the bottom and top parts. The activities of SAI, CWI and NI in both sugarcane species were higher in the top part at each growth stage, lower in middle and lowest in the bottom part of the stem. These activities decreased from 6 to 12 MAP with line 20-2248, whereas the activities increased with increasing time after planting for line S98-244. There was a significantly negative correlation between the sucrose content and the activity of SAI, CWI and NI for line 20-2248. With line S98-244, the lowest concentration of sucrose was significantly negative only with SAI activity. The sucrose content correlation with CWI and with NI activity showed negative correlations but they were not significant. |
หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : A Statistical Approach for Culture Condition Improvement of Invertase and Inulinase from Candida guilliermondii TISTR 5844) ผู้เขียน:ดร.พิลาณี ไวถนอมสัตย์ , มลนพรรษ สงพิมพ์, ดร.สาโรจน์ ศิริศันสนียกุล, ศาสตราจารย์ สื่อสิ่งพิมพ์:pdf AbstractA newly isolated yeast Candida guilliermondii TISTR 5844 was shown to be a good producer of invertase and inulinase in an inexpensive, 48-hour batch fermentation. The enzyme production was performed using an orthogonal array experimental design and software for design and analysis of the experiment, based on the Taguchi method. The optimized medium for producing invertase consisted of 5% inulin, 4.8% NH4Cl and 0.6% MgSO4?7H2O at pH 6. Maximum activity and productivity were achieved at 552.12 U.L-1 and 10.28 U.L-1.hr-1, respectively. Inulinase production was maximized using a medium of 1% inulin, 2.4% NH4Cl and 1.2% MgSO4?7H2O at pH 5. Under optimum conditions, inulinase activity and productivity were achieved at 56.41 U.L-1 and 1.18 U.L-1.hr-1, respectively. The optimal temperature was 30 ?C for both enzymes. |
หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Optimization of Inulinase, Invertase and ?-fructofuranosidase Production from Aspergillus niger TISTR 3570 by the Taguchi Method) ผู้เขียน:ดร.สาโรจน์ ศิริศันสนียกุล, ศาสตราจารย์, มลนพรรษ สงพิมพ์, ดร.พิลาณี ไวถนอมสัตย์ สื่อสิ่งพิมพ์:pdf AbstractThe medium conditions for inulinase, invertase and ?-fructofuranosidase (bFFase) production from Aspergillus niger TISTR 3570 were optimized by the Taguchi method. Production of inulinase was most affected by inulin and the production of invertase and bFFase was most affected by pH. The maximum production of enzymes was achieved by employing a medium containing: inulin (50 g.L-1), yeast extract (12 g.L-1), MgSO4?7H2O (6 g.L-1) and an initial pH of 6. The inulinase was thermostable over a wide temperature range (25–80 ?C) and showed maximum activity at 70 ?C. In addition, activity was stable over the range pH 4–10 and the optimum for enzyme activity was pH 5. In contrast, invertase and bFFase were stable below 55 and 50 ?C, respectively, but showed highest activity at 65 and 60 ?C, respectively. Both enzymes were stable over the range pH 4–9 and had optimum activity at pH 4 for invertase and pH 5 for bFFase. |
หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Enhancement of Inulinase and Invertase Production from a Newly Isolated Candida guilliermondii TISTR 5844) ผู้เขียน:มลนพรรษ สงพิมพ์, ดร.พิลาณี ไวถนอมสัตย์, ดร.วิรัตน์ วาณิชย์ศรีรัตนา, รองศาสตราจารย์ , ดร.สาโรจน์ ศิริศันสนียกุล, ศาสตราจารย์ สื่อสิ่งพิมพ์:pdf AbstractThe optimization of inulinase and invertase production from Candida guilliermondii TISTR 5844 was studied using a central composite design with four factors: pH, temperature, inoculum and substrate concentrations. The most significant factors influencing invertase production were pH and temperature with an R2 value of 0.822 (P < 0.05). Unexpectedly, the R2 value for inulinase production was 0.555 (P > 0.05) and there was no significant influence of the tested factors over the production of inulinase. The results obtained from the experimental design using one factor at a time demonstrated the optimum carbon and nitrogen sources for both enzymes were inulin and NH4Cl, respectively. Optimization by Taguchi methodology further indicated the optimum medium compositions for the production of inulinase (inulin concentration 1%, NH4Cl concentration 2.4%, Mg2SO4•7H2O concentration 1.2% and pH 5) and invertase (inulin concentration 5%, NH4Cl concentration 4.8%, Mg2SO4•7H2O concentration 1.2% and pH 6). |